Host: Insect cells • AA: 691-1139 • Tag: N-terminal His • MW: 50.1 kDa
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Rift Valley Fever Virus Glycoprotein Gc (Strain MP12) (recombinant)

Item No. 40874

Technical Information
Synonyms
  • RVFV Glycoprotein Gc
Purity
≥90% estimated by SDS-PAGE
Endotoxin Testing
<1.0 EU/µg determined by the LAL endotoxin assay
Source
Recombinant RVFV N-terminal His-tagged glycoprotein Gc expressed in insect cells
Amino Acids
691-1139
MW
50.1 kDa
Lyophilized from sterile 20 mM Tris,150 mM sodium chloride, pH 8.0, with 10% glycerol
UniProt Accession №
A2T077
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    Rift Valley fever virus (RVFV) is a single-stranded negative-sense RNA virus, member of the Phlebovirus genus, and mosquito-transmitted pathogen endemic to sub-Saharan Africa and the Arabian peninsula.1,2,3 The tripartite RNA genome of RVFV is composed of three segments: L, which encodes L protein, a single-polypeptide viral RNA-dependent RNA polymerase (RdRp), M, which encodes a single open reading frame (ORF) that produces the envelope glycoproteins Gn and Gc and non-structural proteins NSm and Gn/NSm fusion protein, and S, which is ambisense, encoding the nucleoprotein N in the genomic sense orientation and the non-structural protein and major virulence factor NSs in the antigenomic orientation.3,2 RVFV glycoprotein Gc is a class II membrane fusion protein that mediates viral entry and is composed of three domains: domain I, which is a 10-stranded β-barrel that organizes the glycoprotein structure, β-stranded domain II, and IgC-like domain III.4 Cayman’s RVFV Glycoprotein Gc (Strain MP12) (recombinant) protein consists of 459 amino acids and has a calculated molecular weight of 50.1 kDa.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Wang, X., Hu, C., Ye, W., et alStructure of Rift Valley Fever Virus RNA-dependent RNA polymerase. J. Virol. 96(3), e0171321 (2022).

    2. Faburay, B., Wilson, W., McVey, D.S., et alRift Valley fever virus structural and nonstructural proteins: recombinant protein expression and immunoreactivity against antisera from sheep. Vector Borne Zoonotic Dis. 13(9), 619-629 (2013).

    3. Gaudreault, N.N., Indran, S.V., Balamaran, V., et alMolecular aspects of Rift Valley fever virus and the emergence of reassortants. Virus Genes 55(1), (2019).

    4. Dessau, M., and Modis, Y. Crystal structure of glycoprotein C from Rift Valley fever virus. Proc. Natl. Acad. Sci. USA 110(5), 1696-1701 (2013).